cathepsin-g and Melanoma

cathepsin-g has been researched along with Melanoma* in 1 studies

Other Studies

1 other study(ies) available for cathepsin-g and Melanoma

Article	Year
Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases. FEBS letters, 1994, Sep-26, Volume: 352, Issue:2 The degradation of tenascin purified from human melanoma cells was examined by treatment with matrix metalloproteinases (MMPs) and serine proteinases. Among eight different types of proteinases examined, MMP-1, -3, and -7, cathepsin G and leukocyte elastase could digest tenascin, but MMP-2, MMP-9 and thrombin did not. This suggests that tenascin may be readily catabolized by extracellular matrix-degrading proteinases found in the pathophysiological conditions. Topics: Cathepsin G; Cathepsins; Cell Adhesion Molecules, Neuronal; Extracellular Matrix Proteins; Humans; Leukocyte Elastase; Melanoma; Metalloendopeptidases; Neoplasm Proteins; Pancreatic Elastase; Serine Endopeptidases; Tenascin; Tumor Cells, Cultured	1994

Article

Year

Susceptibility of tenascin to degradation by matrix metalloproteinases and serine proteinases.

FEBS letters, 1994, Sep-26, Volume: 352, Issue:2

The degradation of tenascin purified from human melanoma cells was examined by treatment with matrix metalloproteinases (MMPs) and serine proteinases. Among eight different types of proteinases examined, MMP-1, -3, and -7, cathepsin G and leukocyte elastase could digest tenascin, but MMP-2, MMP-9 and thrombin did not. This suggests that tenascin may be readily catabolized by extracellular matrix-degrading proteinases found in the pathophysiological conditions.

Topics: Cathepsin G; Cathepsins; Cell Adhesion Molecules, Neuronal; Extracellular Matrix Proteins; Humans; Leukocyte Elastase; Melanoma; Metalloendopeptidases; Neoplasm Proteins; Pancreatic Elastase; Serine Endopeptidases; Tenascin; Tumor Cells, Cultured

1994